2dbl: Difference between revisions
New page: left|200px<br /> <applet load="2dbl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dbl, resolution 2.9Å" /> '''MOLECULAR BASIS OF C... |
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'''MOLECULAR BASIS OF CROSS-REACTIVITY AND THE LIMITS OF ANTIBODY-ANTIGEN COMPLEMENTARITY'''<br /> | '''MOLECULAR BASIS OF CROSS-REACTIVITY AND THE LIMITS OF ANTIBODY-ANTIGEN COMPLEMENTARITY'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2DBL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with S5H as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2DBL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=S5H:'>S5H</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DBL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:19:06 2008'' | ||
Revision as of 18:19, 15 February 2008
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MOLECULAR BASIS OF CROSS-REACTIVITY AND THE LIMITS OF ANTIBODY-ANTIGEN COMPLEMENTARITY
OverviewOverview
Two major unanswered questions concerning the specificity of antibodies, are: how do structurally different antigens bind with high affinity to the, same antibody, and what are the limits of the antibody combining site, complementarity and flexibility that contribute to such crossreactivity?, We report here a comparative analysis of the X-ray structures of five, conformationally different steroids in complex with the Fab' fragment of, an anti-progesterone antibody DB3 at 2.7 A. This antibody is unable to, complement completely the shape of the hydrophobic antigen so that, crossreactivity occurs with other ligands without major structural, rearrangements of the binding site. Antigen specificity can be explained, through conserved interactions of DB3 with the steroid D-ring, whereas, some of the crossreactivity is realized through different binding, orientations of the steroid skeleton that place the A-ring into, alternative pockets on the antibody surface. The restricted gene usage of, the VGAM3.8 family in the generation of anti-progesterone monoclonal, antibodies may be explained by the specific interaction of VH hallmark, residues with the steroid D-ring. This first detailed structure of steroid, interactions with a protein could be applied to the understanding of, general mechanisms of steroid recognition as well as in the design of, specific binding sites for small hydrophobic ligands.
About this StructureAbout this Structure
2DBL is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Molecular basis of crossreactivity and the limits of antibody-antigen complementarity., Arevalo JH, Taussig MJ, Wilson IA, Nature. 1993 Oct 28;365(6449):859-63. PMID:8413674
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